Premium
Conformational behavior of the linear hexapeptide senktide: A receptor specific tachykinin analog
Author(s) -
Sumner Susan C.J.,
Ferretti James A.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80942-1
Subject(s) - antiparallel (mathematics) , steric effects , tachykinin receptor , chemistry , receptor , stereochemistry , biophysics , biochemistry , biology , neuropeptide , substance p , physics , quantum mechanics , magnetic field
A receptor selective linear hexapeptide tachykinin analog, senktide, is shown to be highly ordered in solution. The conformational restriction is attributed to steric and electrostatic interactions produced by N ‐methylation of the third amino acid residue in the sequence and the negatively charged N‐terminus. The structure of senktide is described as a dynamic mixture of similar conformations where the predominant one is a distorted antiparallel hydrogen bonded β‐pleated sheet. The observed senktide‐receptor specificity is suggested to result from a selection of this or a closely related conformation.